ID   UBC2_CANAL              Reviewed;         179 AA.
AC   O74201; Q5A0A0;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 56.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 2;
DE            EC=6.3.2.19;
DE   AltName: Full=Ubiquitin-protein ligase UBC2;
DE   AltName: Full=Ubiquitin carrier protein UBC2;
DE   AltName: Full=Radiation sensitivity protein 6;
GN   Name=UBC2; Synonyms=RAD6; ORFNames=CaO19.7195;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=3153A;
RA   Leng P., Brown A.J.P.;
RT   "Molecular cloning and characterisation of CaRAD6 gene from Candida
RT   albicans.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=3153A;
RX   MEDLINE=20177840; PubMed=10712706;
RX   DOI=10.1046/j.1365-2958.2000.01801.x;
RA   Leng P., Sudbery P.E., Brown A.J.P.;
RT   "Rad6p represses yeast-hypha morphogenesis in the human fungal
RT   pathogen Candida albicans.";
RL   Mol. Microbiol. 35:1264-1275(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
RA   Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
RA   Davis R.W., Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Plays a role in transcription regulation by catalyzing
CC       the monoubiquitination of histone H2B to form H2BK123ub1.
CC       H2BK123ub1 gives a specific tag for epigenetic transcriptional
CC       activation and is also a prerequisite for H3K4me and H3K79me
CC       formation. Also involved in postreplication repair of UV-damaged
CC       DNA, in N-end rule-dependent protein degradation and in
CC       sporulation (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- INDUCTION: Up-regulated by UV radiation, heat shock, osmotic
CC       stress and nitrogen starvation.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAK96213.1; Type=Erroneous gene model prediction;
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DR   EMBL; AF036707; AAC24765.1; -; mRNA.
DR   EMBL; AF118145; AAD45241.1; -; Genomic_DNA.
DR   EMBL; AACQ01000089; EAK96213.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_715243.1; -.
DR   HSSP; P06104; 1AYZ.
DR   SMR; O74201; 2-154.
DR   GeneID; 3643143; -.
DR   KEGG; cal:CaO19.7195; -.
DR   CGD; CAL0003164; RAD6.
DR   BRENDA; 6.3.2.19; 1124.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0019941; P:modification-dependent protein catabolic pr...; IEA:UniProtKB-KW.
DR   GO; GO:0043687; P:post-translational protein modification; IEA:InterPro.
DR   GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cel...; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR016135; UBQ-conjugat/RWD-like.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   ProDom; PD000461; UBQ_conjugat; 1.
DR   SMART; SM00212; UBCc; 1.
DR   PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chromatin regulator; Cytoplasm; DNA damage; DNA repair;
KW   Ligase; Nucleotide-binding; Nucleus; Sporulation; Transcription;
KW   Transcription regulation; Ubl conjugation pathway.
FT   CHAIN         1    179       Ubiquitin-conjugating enzyme E2 2.
FT                                /FTId=PRO_0000082528.
FT   REGION      151    179       Acidic tail.
FT   ACT_SITE     88     88       Glycyl thioester intermediate (By
FT                                similarity).
SQ   SEQUENCE   179 AA;  20576 MW;  24A081B5F8E4D316 CRC64;
     MSTPARRRLM RDFKRMQQDP PSGVSASPLP DNVMKWNAVI IGPSDTPFED GTFRLLLSFD
     EQYPNKPPQV KFISEMFHPN VYASGELCLD ILQNRWSPTY DVSSILTSVQ SLLNDPNISS
     PANVEAANLY KDHRSLYVKR VRETVENSWN DDDDEEEEEE DEDEAEDEDD DDDDNIDED
//